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606839

Sigma-Aldrich

ISOGRO®-13C,15N Powder -Growth Medium

98 atom % 15N, 99 atom % 13C

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About This Item

MDL number:
MFCD00197704
UNSPSC Code:
12352200
NACRES:
NA.12

isotopic purity

99 atom % 13C
98 atom % 15N

Quality Level

200

form

solid

technique(s)

bio NMR: suitable
protein expression: suitable

storage temp.

−20°C

Packaging

This product may be available from bulk stock and can be packaged on demand. For information on pricing, availability and packaging, please contact Stable Isotopes Customer Service.

Legal Information

ISOGRO is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Certificates of Analysis (COA)

Lot/Batch Number
MBBD3293
MBBC7360
MBBC4464
EB2252
TA0407V

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Sigma-Aldrich

364584

Nitrogen-15N2

Glass beads, acid-washed 425-600 μm (30-40 U.S. sieve)

Sigma-Aldrich

G8772

Glass beads, acid-washed

Nicholas C Fitzkee et al.
The Journal of biological chemistry, 285(23), 18072-18084 (2010-04-07)
The human immunodeficiency virus type 1 (HIV-1) integrase (IN) is a critical enzyme involved in infection. It catalyzes two reactions to integrate the viral cDNA into the host genome, 3' processing and strand transfer, but the dynamic behavior of the
J L Urbauer et al.
The Journal of biological chemistry, 276(44), 41128-41132 (2001-08-24)
The association of the bacteriophage T4-encoded AsiA protein with the final sigma(70) subunit of the Escherichia coli RNA polymerase is one of the principal events governing transcription of the T4 genome. Analytical ultracentrifugation and NMR studies indicate that free AsiA
Ara Celi DiCostanzo et al.
The Journal of biological chemistry, 287(33), 27997-28006 (2012-06-29)
Light chain amyloidosis is an incurable protein misfolding disease where monoclonal immunoglobulin light chains misfold and deposit as amyloid fibrils, causing organ failure and death. Previously, we determined that amyloidogenic light chains AL-09 and AL-103 do not form fibrils at
Xavier Hanoulle et al.
The Journal of biological chemistry, 284(20), 13589-13601 (2009-03-20)
We report here a biochemical and structural characterization of domain 2 of the nonstructural 5A protein (NS5A) from the JFH1 Hepatitis C virus strain and its interactions with cyclophilins A and B (CypA and CypB). Gel filtration chromatography, circular dichroism
Christian Koehler et al.
The Journal of biological chemistry, 286(17), 14842-14851 (2011-03-04)
NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the family of ADP-ribosyltransferases (ADPRT) and catalyzes the transfer of ADP-ribose moieties to arginine residues in target protein acceptors.
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